ID   MSRQ_POLNA              Reviewed;         219 AA.
AC   A1VK09;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ {ECO:0000255|HAMAP-Rule:MF_01207};
DE   AltName: Full=Flavocytochrome MsrQ {ECO:0000255|HAMAP-Rule:MF_01207};
GN   Name=msrQ {ECO:0000255|HAMAP-Rule:MF_01207}; OrderedLocusNames=Pnap_0668;
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2;
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(2009).
CC   -!- FUNCTION: Part of the MsrPQ system that repairs oxidized periplasmic
CC       proteins containing methionine sulfoxide residues (Met-O), using
CC       respiratory chain electrons. Thus protects these proteins from
CC       oxidative-stress damage caused by reactive species of oxygen and
CC       chlorine generated by the host defense mechanisms. MsrPQ is essential
CC       for the maintenance of envelope integrity under bleach stress, rescuing
CC       a wide series of structurally unrelated periplasmic proteins from
CC       methionine oxidation. MsrQ provides electrons for reduction to the
CC       reductase catalytic subunit MsrP, using the quinone pool of the
CC       respiratory chain. {ECO:0000255|HAMAP-Rule:MF_01207}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01207};
CC       Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01207};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01207};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_01207};
CC   -!- SUBUNIT: Heterodimer of a catalytic subunit (MsrP) and a heme-binding
CC       subunit (MsrQ). {ECO:0000255|HAMAP-Rule:MF_01207}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01207}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01207}.
CC   -!- SIMILARITY: Belongs to the MsrQ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01207}.
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DR   EMBL; CP000529; ABM35987.1; -; Genomic_DNA.
DR   RefSeq; WP_011800082.1; NC_008781.1.
DR   AlphaFoldDB; A1VK09; -.
DR   STRING; 365044.Pnap_0668; -.
DR   EnsemblBacteria; ABM35987; ABM35987; Pnap_0668.
DR   KEGG; pna:Pnap_0668; -.
DR   eggNOG; COG2717; Bacteria.
DR   HOGENOM; CLU_080662_0_0_4; -.
DR   OMA; LHFFWMR; -.
DR   OrthoDB; 1508607at2; -.
DR   Proteomes; UP000000644; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01207; MsrQ; 1.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR022837; MsrQ-like.
DR   PANTHER; PTHR36964; PTHR36964; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Electron transport; Flavoprotein; FMN;
KW   Heme; Iron; Membrane; Metal-binding; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..219
FT                   /note="Protein-methionine-sulfoxide reductase heme-binding
FT                   subunit MsrQ"
FT                   /id="PRO_1000164664"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
SQ   SEQUENCE   219 AA;  24855 MW;  CA8D13F0280CCA9B CRC64;
     MAAWMAGRQK WLLHPAAKPL IFMVCLLPFA WLFYAAWSDQ LGANPAEALV RATGDWTLRF
     VCIVLAVTPL RVITRTPALA RFRRMLGLFA YFYVVLHLLS YSWFDMGFDV ADIARDIAKR
     PFILVGFSAF VLLTPLAATS FNAAIKAMGA KRWQLLHKLV YLIAGLGLLH FFWMRAGKNN
     FNEVFVYAAI VALLLGWRVW NHWAKARRRV SNNAAVGVH